Dr. Slyviane Muller, founder of Lupuzor, presents at Osaka University, Japan
23rd April 2014 - 11:02 amImmuPharma PLC (LSE: IMM), (“ImmuPharma” or the “Company”), the specialist drug discovery and development company, is pleased to announce that Dr. Sylviane Muller was recently invited by the Immunology Frontier Research Center of Osaka University, an internationally renowned research center in the field of immunology, to hold a seminar on the approach of Lupuzor for treating lupus patients. The details of her abstract have now been released.
Dr. Sylviane Muller, Research Director at CNRS, Strasbourg, France is the key inventor of Lupuzor. Her abstract was titled “Chaperone-mediated autophagy as a target of therapeutic P140 peptide used in lupus”. Her presentation focused partly on the on the highly competitive and efficacious mode of mechanism of LupuzorTM (also known scientifically as P140), ImmuPharma’s potential blockbuster drug for Lupus, a chronic autoimmune disease. LupuzorTM has received Special Protocol Assessment and Fast Track Designation from the FDA for a Phase III trial.
Sylviane Muller’s Abstract : Summary
“In the pipeline of molecules with a potential for treating lupus patients, the P140 peptide holds a lot of promise. P140 is a 21-mer linear peptide (sequence 131-151) derived from the spliceosomal small nuclear ribonucleoprotein U1-70K. It contains a phosphoserine residue at position 140. In a multicenter, randomized, placebo-controlled phase IIb study, P140/Lupuzor was safe and met its primary efficacy end points in lupus patients (Zimmer et al., ARD 2013). These results confirm data generated in MRL/lpr lupus-prone mice in which the preclinical studies were conducted (Monneaux et al., EJI 2003; Schall et al., J Autoimmunity 2012). In this setting, as in human, P140 was shown to behave as an immunomodulator and not as an immunosuppressant. In a step further, our studies demonstrated that the P140 peptide mechanism of action does involve autophagy processes. In a lupus context in which macroautophagy is affected (Gros et al., 2012), P140 readily binds HSPA8/HSC70 chaperone proteins (Page et al., PLoS ONE 2009) and reduces autophagic flux in MRL/lpr B cells (Page et al., ARD 2011). We recently showed that a selective form of autophagy, chaperone-mediated autophagy (CMA), is a key target of P140. By interfering with this particular pathway, P140 peptide may affect the endogenous (auto)antigen processing and the peptide loading to MHCII molecules, and as a consequence, induces a lower activation of autoreactive T and B cells, and a reduction of autoantibodies secreted by plasma cells. Our recent results shed light on mechanisms by which P140 can modulate lupus disease and by which it may operate in humans affected by this disorder that affect more than 5 million individuals in the world”.